|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-424 |
0e+00 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 654.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 2 AKNIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEvtDVVEKEMYTFEDRNGDSLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 82 PEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 162 TLELNSIGSLEARAnyrDALVAFLE-----QHKEKLDEDCKRRMYTNPLR-VLDSKNPEVQALLNDAPALGDYLDEESRE 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 236 HFAGLCKLLESAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 316 VQAVNPEFKADPVVDIYLVASGADTQSAAMALAERLRDElpGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANG 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....*....
1KMM_D 396 TAVVKDLRSGEQTAVAQDSVAAHLRTLLG 424
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-412 |
0e+00 |
|
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273080 [Multi-domain] Cd Length: 404 Bit Score: 637.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 6 QAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 86 AGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHVTLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 166 NSIGSLEARANYRDALVAFLEQHKEKLDEDCKRRMYTNPLRVLDSKNPEVQALLNDAPALGDYLDEESREHFAGLCKLLE 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 246 SAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQAVNPEFKA 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 326 DPVVDIYLVASGADTQSAAMALAERLRDElpGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSG 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
1KMM_D 406 EQTAVAQ 412
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-407 |
5.81e-144 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 416.99 E-value: 5.81e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 1 MAKnIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 81 RPEGTAGCVRAGIEHGLLY-NQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGISE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 160 HVtLELNSIGSLEARANYRDALVAFLEQHKEKLDEDCKRRMYTNPLRVLDSKNPEVQALLNDAPALGDYLDEESREHFAG 239
Cdd:CHL00201 160 LI-LDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 240 LCKLLESAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ-- 317
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKdn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 318 AVNPEFKadpvVDIYLVASGADTQSAAMALAERLRDELpgVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTA 397
Cdd:CHL00201 319 IILPKQS----IDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCI 392
|
410
....*....|
1KMM_D 398 VVKDLRSGEQ 407
Cdd:CHL00201 393 TIKWLDEQVQ 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
4.87e-106 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 314.16 E-value: 4.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 18 ETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRaigEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 98 LYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHVTLELNSIGSLEARANy 177
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 178 rdalvafleqhkekldedckrrmytnplrvlDSKNPEVQALlndapALGDYLDEESREHFAGLCKLLESAG--IAYTVNQ 255
Cdd:cd00773 156 -------------------------------LLEDREEYIE-----RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDL 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
1KMM_D 256 RLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ 317
Cdd:cd00773 200 SLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
1.59e-39 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 143.88 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDvvekEMYTFEDRNGDSLTLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 90 RAgIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHVTLELNSIG 169
Cdd:pfam13393 77 RI-DAHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 170 -------SLEARANYRDALVAFLEQHK-EKLDEdCKRRMYTNP-----LRVLDSKNPEVQALLNDAPAL-GDYLDEESRE 235
Cdd:pfam13393 155 lvralleAAGLSEALEEALRAALQRKDaAELAE-LAAEAGLPPalrraLLALPDLYGGPEVLDEARAALpGLPALQEALD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1KMM_D 236 HFAGLCKLLESAG--IAYTVNQRLVRGLDYYNRTVFEWVTnsLGSQGTVCAGGRYDGLVEQLgGRATPAVGFAMGLERL 312
Cdd:pfam13393 234 ELEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYA--PGVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-424 |
0e+00 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 654.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 2 AKNIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEvtDVVEKEMYTFEDRNGDSLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 82 PEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 162 TLELNSIGSLEARAnyrDALVAFLE-----QHKEKLDEDCKRRMYTNPLR-VLDSKNPEVQALLNDAPALGDYLDEESRE 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 236 HFAGLCKLLESAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 316 VQAVNPEFKADPVVDIYLVASGADTQSAAMALAERLRDElpGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANG 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....*....
1KMM_D 396 TAVVKDLRSGEQTAVAQDSVAAHLRTLLG 424
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-412 |
0e+00 |
|
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273080 [Multi-domain] Cd Length: 404 Bit Score: 637.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 6 QAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 86 AGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHVTLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 166 NSIGSLEARANYRDALVAFLEQHKEKLDEDCKRRMYTNPLRVLDSKNPEVQALLNDAPALGDYLDEESREHFAGLCKLLE 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 246 SAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQAVNPEFKA 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 326 DPVVDIYLVASGADTQSAAMALAERLRDElpGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSG 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
1KMM_D 406 EQTAVAQ 412
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-407 |
5.81e-144 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 416.99 E-value: 5.81e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 1 MAKnIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 81 RPEGTAGCVRAGIEHGLLY-NQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGISE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 160 HVtLELNSIGSLEARANYRDALVAFLEQHKEKLDEDCKRRMYTNPLRVLDSKNPEVQALLNDAPALGDYLDEESREHFAG 239
Cdd:CHL00201 160 LI-LDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 240 LCKLLESAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ-- 317
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKdn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 318 AVNPEFKadpvVDIYLVASGADTQSAAMALAERLRDELpgVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTA 397
Cdd:CHL00201 319 IILPKQS----IDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCI 392
|
410
....*....|
1KMM_D 398 VVKDLRSGEQ 407
Cdd:CHL00201 393 TIKWLDEQVQ 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
4.87e-106 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 314.16 E-value: 4.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 18 ETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRaigEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 98 LYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHVTLELNSIGSLEARANy 177
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 178 rdalvafleqhkekldedckrrmytnplrvlDSKNPEVQALlndapALGDYLDEESREHFAGLCKLLESAG--IAYTVNQ 255
Cdd:cd00773 156 -------------------------------LLEDREEYIE-----RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDL 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
1KMM_D 256 RLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ 317
Cdd:cd00773 200 SLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
18-317 |
4.76e-49 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 166.80 E-value: 4.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 18 ETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIgeVTDVVEKEMYTFEDRN----GDSLTLRPEGTAGCVRAGI 93
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG--HLDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 94 EHGLLY-NQEQRLWYIGPMFRHERPQ---KGRYRQFHQLGCEVFGLQG--PDIDAELIMLTARWWRALGisEHVTLELNS 167
Cdd:cd00670 79 GEILSYrALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEeaEEERREWLELAEEIARELG--LPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 168 IGSLEARANyrdalvafleqhkekldedckrrmytnplrvldsknpevqallndapalgdyldeesrehfaglckllesa 247
Cdd:cd00670 157 DPFFGRGGK----------------------------------------------------------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 248 giaytvnqrlvRGLDYYNRTVFEWVTNSL--GSQGTVCAGGRYDGLVEQ---------LGGRATPAVGFAMGLERLVLLV 316
Cdd:cd00670 166 -----------RGLDAGRETVVEFELLLPlpGRAKETAVGSANVHLDHFgasfkidedGGGRAHTGCGGAGGEERLVLAL 234
|
.
1KMM_D 317 Q 317
Cdd:cd00670 235 L 235
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
13-317 |
2.70e-46 |
|
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273081 [Multi-domain] Cd Length: 313 Bit Score: 161.63 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 13 DYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEqtplFKRAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAG 92
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLE----YLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 93 IEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGISEhVTLEL------- 165
Cdd:TIGR00443 78 STRLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKD-FKIELghvglvr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 166 ----NSIGSLEARANYRDAL----VAFLEQHKEKLDEDCKRRMYTNPLRVLDSKNPEV----QALLNDAPALGdYLDEES 233
Cdd:TIGR00443 157 alleEAGLPEEAREALREALarkdLVALEELVAELGLSPEVRERLLALPRLRGDGEEVleeaRALAGSETAEA-ALDELE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 234 RehfagLCKLLESAGI--AYTVNQRLVRGLDYYNRTVFEWVTNSLGSqgTVCAGGRYDGLVEQLgGRATPAVGFAMGLER 311
Cdd:TIGR00443 236 A-----VLELLEARGVeeYISLDLGLVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYDELLGRF-GRPLPATGFALNLER 307
|
....*.
1KMM_D 312 LVLLVQ 317
Cdd:TIGR00443 308 LLEALT 313
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
9-414 |
1.09e-43 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 159.14 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 9 RGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGE-VTDvvekEMYTFEDRNGDSLTLRPEGTAG 87
Cdd:PLN02530 74 KGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEeITD----QLYNFEDKGGRRVALRPELTPS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 88 CVRAGIEHGllynQEQRL---WY-IGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGI-SEHVT 162
Cdd:PLN02530 150 LARLVLQKG----KSLSLplkWFaIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGItSSDVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 163 LELNSIGSLEARANYRD------ALVAFLEQHKEKLdedcKRRMYTNPLRVLDSKNPEVQALLN-----DAPALGDYLDE 231
Cdd:PLN02530 226 IKVSSRKVLQAVLKSYGipeesfAPVCVIVDKLEKL----PREEIEKELDTLGVSEEAIEGILDvlslkSLDDLEALLGA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 232 ESrEHFAGLCKLLESA---GIA--YTVNQRLVRGLDYYNRTVFEWVTNSlGSQGTVCAGGRYDGLVEQLGGRATPAVGFA 306
Cdd:PLN02530 302 DS-EAVADLKQLFSLAeayGYQdwLVFDASVVRGLAYYTGIVFEGFDRA-GKLRAICGGGRYDRLLSTFGGEDTPACGFG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 307 MGLERLVLLVQ--AVNPEFKadPVVDIYLVASGADTQSAAMALAERLRDELPGVKLMTNhgGGNFKKQFARADKWGARVA 384
Cdd:PLN02530 380 FGDAVIVELLKekGLLPELP--HQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLE--PKKLKWVFKHAERIGAKRL 455
|
410 420 430
....*....|....*....|....*....|
1KMM_D 385 VVLGESEVANGTAVVKDLRSGEQTAVAQDS 414
Cdd:PLN02530 456 VLVGASEWERGMVRVKDLSSGEQTEVKLDE 485
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-354 |
4.15e-43 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 155.41 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGevtDVVEKEMYTFEDR-NGDSLTLRPEGTAGC 88
Cdd:PRK12292 8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGG---AILDLRTFKLVDQlSGRTLGLRPDMTAQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 89 VRAgIEHGLLYNQE-QRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGISEhVTLEL-- 165
Cdd:PRK12292 85 ARI-AATRLANRPGpLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPN-FTLDLgh 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 166 ---------NSIGSLEARANYRDALVAF----LEQHKEKLDEDCKR------RMYtNPLRVLDsknpEVQALLNDAPALg 226
Cdd:PRK12292 163 vglfralleAAGLSEELEEVLRRALANKdyvaLEELVLDLSEELRDallalpRLR-GGREVLE----EARKLLPSLPIK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 227 dyldeESREHFAGLCKLLESAGIAYTVNQRL--VRGLDYYNRTVFEWVTNSLGSQgtVCAGGRYDGLVEQLgGRATPAVG 304
Cdd:PRK12292 237 -----RALDELEALAEALEKYGYGIPLSLDLglLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRF-GRARPATG 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
1KMM_D 305 FAMGLERLVLLVQAVNPefkadPVVDIYLVASGADTQSAAMALAERLRDE 354
Cdd:PRK12292 309 FSLDLDRLLELQLELPV-----EARKDLVIAPDSEALAAALAAAQELRKK 353
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
1.59e-39 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 143.88 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDvvekEMYTFEDRNGDSLTLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 90 RAgIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHVTLELNSIG 169
Cdd:pfam13393 77 RI-DAHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 170 -------SLEARANYRDALVAFLEQHK-EKLDEdCKRRMYTNP-----LRVLDSKNPEVQALLNDAPAL-GDYLDEESRE 235
Cdd:pfam13393 155 lvralleAAGLSEALEEALRAALQRKDaAELAE-LAAEAGLPPalrraLLALPDLYGGPEVLDEARAALpGLPALQEALD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1KMM_D 236 HFAGLCKLLESAG--IAYTVNQRLVRGLDYYNRTVFEWVTnsLGSQGTVCAGGRYDGLVEQLgGRATPAVGFAMGLERL 312
Cdd:pfam13393 234 ELEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYA--PGVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-318 |
1.76e-39 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 143.78 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 15 LPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDvveKEMYTFEDRNGDSLTLRPEGTAGCVRAGIE 94
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARIAAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 95 HglLYNQE--QRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEHVTLELNSIG--- 169
Cdd:COG3705 78 R--LANRPgpLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGL-EDFTLDLGHVGlfr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 170 ----SLEARANYRDALVAFLEQ----------HKEKLDEDCKRRMY-----TNPLRVLDsknpEVQALLNDAPALgdyld 230
Cdd:COG3705 155 alleALGLSEEQREELRRALARkdaveleellAELGLSEELAEALLalpelYGGEEVLA----RARALLLDAAIR----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 231 eESREHFAGLCKLLESAGIA--YTVNQRLVRGLDYYNRTVFEWVTNSLGsqGTVCAGGRYDGLVEQLgGRATPAVGFAMG 308
Cdd:COG3705 226 -AALDELEALAEALAARGPDvrLTFDLSELRGYDYYTGIVFEAYAPGVG--DPLARGGRYDGLLAAF-GRARPATGFSLD 301
|
330
....*....|
1KMM_D 309 LERLVLLVQA 318
Cdd:COG3705 302 LDRLLRALPA 311
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
21-173 |
5.23e-39 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 139.56 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 21 IWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEvtdvvEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHglLYN 100
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE-----PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH--IRK 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1KMM_D 101 QEQRLWYIGPMFRHERPQKG--RYRQFHQLGCEVFGLQGPD--IDAELIMLTARWWRALGISEHVTLELNSIGSLEA 173
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEasEFEELIELTEELLRALGIKLDIVFVEKTPGEFSP 150
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
6-415 |
3.44e-36 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 137.55 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 6 QAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLF--KRAIGevtDVVEKEMYTFEDRNGDSLTLRPE 83
Cdd:PRK12420 5 RNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMssKYGGG---DEILKEIYTLTDQGKRDLALRYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 84 GTAGCVRAgiehgLLYNQEQRLWY----IGPMFRHERPQKGRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGISe 159
Cdd:PRK12420 82 LTIPFAKV-----VAMNPNIRLPFkryeIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 160 hVTLELNSIGSL-----EARANYRDALVAFLEQHK-EKLDEDCKRrmytNPLRVLDSKNPEVQALLNDAPALGDYLDEES 233
Cdd:PRK12420 156 -VTIQYNNRKLLngilqAIGIPTELTSDVILSLDKiEKIGIDGVR----KDLLERGISEEMADTICNTVLSCLQLSIADF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 234 REHFAG------------LCKLLESAGIA--YTVNQRLVRGLDYYNRTVFEW------VTNSLGSqgtvcaGGRYDGLVE 293
Cdd:PRK12420 231 KEAFNNplvaegvnelqqLQQYLIALGINenCIFNPFLARGLTMYTGTVYEIflkdgsITSSIGS------GGRYDNIIG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 294 QLGG--RATPAVGFAMGLErlvLLVQAVNPEFKADPVVDIYLVASGadTQSAAMALAERLRdELPGVKLMTNHGGGNFKK 371
Cdd:PRK12420 305 AFRGddMNYPTVGISFGLD---VIYTALSQKETISSTADVFIIPLG--TELQCLQIAQQLR-STTGLKVELELAGRKLKK 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....
1KMM_D 372 QFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQTAVAQDSV 415
Cdd:PRK12420 379 ALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
68-320 |
4.12e-36 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 130.61 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 68 YTFEDRNGDSLTLRPEGTAGCVRAGIEHGL-LYNQEQRLWYIGPMFRHERP--QKG--RYRQFHQLGCEVFGLQG--PDI 140
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLrSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGqsPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 141 DAELIMLTARWWRALGISEHVTLELNSIGSlearanyrdalvafleqhkekldedckrrmytnplrvldsknpevqalln 220
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGS-------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 221 dapalgdyldeesrehfaglckllesagiaytvnqrlvrgLDYYNRTVFEWVTNSLGSQG-TVCAGGRYDGLVEQLGGRA 299
Cdd:pfam00587 111 ----------------------------------------AFYGPKLDFEVVFPSLGKQRqTGTIQNDGFRLPRRLGIRY 150
|
250 260 270
....*....|....*....|....*....|.
1KMM_D 300 --------TP-AVGFA-MGLERLVLLVQAVN 320
Cdd:pfam00587 151 kdedneskFPyMIHRAgLGVERFLAAILENN 181
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
328-420 |
1.99e-30 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 112.63 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 328 VVDIYLVASGADTQSAAMALAERLRDElpGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQ 407
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDA--GIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQ 78
|
90
....*....|...
1KMM_D 408 TAVAQDSVAAHLR 420
Cdd:cd00859 79 ETVALDELVEELK 91
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
9-423 |
6.98e-27 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 113.44 E-value: 6.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 9 RGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTdvveKEMYTFEDRNGDSLTLRPEGTAGC 88
Cdd:PLN02972 331 KGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDS----KLIYDLADQGGELCSLRYDLTVPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 89 VRAGIEHGLlynQEQRLWYIGPMFRHERPQKGRYRQFHQLGCEVFGLQGP-DIDAELIMLtarwwralgISEHVTlELNs 167
Cdd:PLN02972 407 ARYVAMNGI---TSFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIKV---------LTELLD-ELD- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 168 IGSLEARANYRDALVAFLE-------------QHKEKLD----EDCKRRMYTN---PLRVLD-------SKNPEVQALLN 220
Cdd:PLN02972 473 IGTYEVKLNHRKLLDGMLEicgvppekfrticSSIDKLDkqsfEQVKKEMVEEkglSNETADkignfvkERGPPLELLSK 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 221 ----DAPALGDYLDEESREHFAGLCKLLESAGI--AYTVNQRLVRGLDYYNRTVFEWVTNslGSQ-GTVCAGGRYDGLVE 293
Cdd:PLN02972 553 lrqeGSEFLGNASSRAALDELEIMFKALEKSKAigKIVFDLSLARGLDYYTGVIYEAVFK--GAQvGSIAAGGRYDNLVG 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 294 QLGGRATPAVGFAMGLERLVLLVQAVNPEFKAD--PVVDIYLVAS-GADTQSAAMALAERL-----RDELPGVKLMTNHg 365
Cdd:PLN02972 631 MFSGKQVPAVGVSLGIERVFAIMEQQEEEKSQVirPTETEVLVSIiGDDKLALAAELVSELwnagiKAEYKVSTRKAKH- 709
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
1KMM_D 366 ggnfkkqFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQTAVAQDSVAAHLRTLL 423
Cdd:PLN02972 710 -------LKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
65-318 |
6.37e-16 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 78.82 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 65 KEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGLlyNQEQRLWYIGPMFRHerpQKGRYRQFHQLGCEVFGLQGP-DIDAE 143
Cdd:PRK12295 47 RRIFVTSDENGEELCLRPDFTIPVCRRHIATAG--GEPARYAYLGEVFRQ---RRDRASEFLQAGIESFGRADPaAADAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 144 LIMLTARWWRALGISEhVTLELNSIGSLEA--------------------RANYRDALVAFL--------EQHKEKL--- 192
Cdd:PRK12295 122 VLALALEALAALGPGD-LEVRLGDVGLFAAlvdalglppgwkrrllrhfgRPRSLDALLARLagprvdplDEHAGVLaal 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 193 -DEDCKRRMYTNPL------------------RVL--------DSKNPEVQALLNDAPALGDYLDEESR--EHFAGLCKL 243
Cdd:PRK12295 201 aDEAAARALVEDLMsiagispvggrspaeiarRLLekaalaaaARLPAEALAVLERFLAISGPPDAALAalRALAADAGL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 244 ---------------LESAGIA---YTVNQRLVRGLDYYNRTVFEWVTNSLGSqGTVCAGGRYDGLVEQLG-GRATPAVG 304
Cdd:PRK12295 281 dldaaldrfearlaaLAARGIDlerLRFSASFGRPLDYYTGFVFEIRAAGNGD-PPLAGGGRYDGLLTRLGaGEPIPAVG 359
|
330
....*....|....
1KMM_D 305 FAMGLERLVLLVQA 318
Cdd:PRK12295 360 FSIWLDRLAALGGA 373
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-354 |
3.62e-10 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 61.14 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVekemyTFedRNGDSLTLRPEGtagcV 89
Cdd:PRK12421 12 GVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQ-----TF--KLIDQLSGRLMG----V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 90 RAGI--------EHGLLYNQEQRLWYIGPMFrHERPQK-GRYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGIsEH 160
Cdd:PRK12421 81 RADItpqvaridAHLLNREGVARLCYAGSVL-HTLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGV-PA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 161 VTLELNSIG---SLEARA----NYRDALVAFLeQHKE--KLDEDCKRRMYTNPLR----VLDSKNPEVQALLNDAPALGD 227
Cdd:PRK12421 159 LHLDLGHVGifrRLAELAglspEEEEELFDLL-QRKAlpELAEVCQNLGVGSDLRrmfyALARLNGGLEALDRALSVLAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 228 YlDEESREHFAGLCKLLESAGIAYT---VNQRLV--RGLDYYNRTVFEWVTNSLGSQgtVCAGGRYDGlVEQLGGRATPA 302
Cdd:PRK12421 238 Q-DAAIRQALDELKTLAAHLKNRWPelpVSIDLAelRGYHYHTGLVFAAYIPGRGQA--LARGGRYDG-IGEAFGRARPA 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
1KMM_D 303 VGFAMGLERLVLLVQAVnPEFKAdpvvdiyLVASGADTQSAAMALAErLRDE 354
Cdd:PRK12421 314 TGFSMDLKELLALQFLE-EEAGA-------ILAPWGDDPDLLAAIAE-LRQQ 356
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
328-422 |
6.15e-10 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 55.67 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 328 VVDIYLVASGADTQSAAMALAERLRDElpGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQ 407
Cdd:pfam03129 2 VVVIPLGEKAEELEEYAQKLAEELRAA--GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
1KMM_D 408 TAVAQDSVAAHLRTL 422
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
329-420 |
1.04e-07 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 49.32 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 329 VDIYLVASGADTQSAaMALAERLRDEL--PGVKLMTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSGE 406
Cdd:cd00738 2 IDVAIVPLTDPRVEA-REYAQKLLNALlaNGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
90
....*....|....
1KMM_D 407 QTAVAQDSVAAHLR 420
Cdd:cd00738 81 SETLHVDELPEFLV 94
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
17-307 |
1.06e-06 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 49.99 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 17 GETA-IWQRIEGTLKNVLGSYGYSEIrlpiveQTPLFKRAIGE-VTDvvEKEMYTFEDRNGDSLTLRPEGTAGCVRAgIE 94
Cdd:PRK12293 16 GKSAkLKREIENVASEILYENGFEEI------VTPFFSYHQHQsIAD--EKELIRFSDEKNHQISLRADSTLDVVRI-VT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 95 HGLLYNQEQRLW-YIGPMFRHerPQkgryRQFHQLGCEVFGlqGPDIdAELIMLTARWWRALGISEHVTLELNSIGSLEA 173
Cdd:PRK12293 87 KRLGRSTEHKKWfYIQPVFRY--PS----NEIYQIGAELIG--EEDL-SEILNIAAEIFEELELEPILQISNIKIPKLVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 174 RaNYRDALVAFLEQHKEKLDEdcKRRMYTNPLRVLdsKNPE-VQALLNDAPalgDYLDEEsrehfagLCKLLESA-GIAY 251
Cdd:PRK12293 158 E-ILGLDIEVFKKGQIEKLLA--QNVPWLNKLVRI--KTLEdLDEVIELVP---DEIKEE-------LEKLKELAeSIKY 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
1KMM_D 252 TvNQRLV----RGLDYYNRTVFEWVTNSLgsqgTVCAGGRY--DGLveqlggratPAVGFAM 307
Cdd:PRK12293 223 E-NLVIAplyyAKMRYYDDLFFRFFDGNS----TLASGGNYeiDGI---------SSSGFAL 270
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
343-424 |
5.32e-04 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 42.38 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 343 AAMALAERL---------------RDELPGVKlmtnhgggnfkkqFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQ 407
Cdd:PRK09194 482 EVKELAEKLyaelqaagievllddRKERPGVK-------------FADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEK 548
|
90
....*....|....*..
1KMM_D 408 TAVAQDSVAAHLRTLLG 424
Cdd:PRK09194 549 EEVPVDELVEFLKALKK 565
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
10-133 |
5.98e-03 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 38.30 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KMM_D 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKraIGEVTDVVEKEMYTFEdRNGDSLTLRPegtAGCV 89
Cdd:cd00771 21 GLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWE--TSGHWDHYRENMFPFE-EEDEEYGLKP---MNCP 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
1KMM_D 90 ragiEHGLLYNQEQRLWY--------IGPMFRHErpQKG------RYRQFHQLGCEVF 133
Cdd:cd00771 95 ----GHCLIFKSKPRSYRdlplrlaeFGTVHRYE--QSGalhgltRVRGFTQDDAHIF 146
|
|
| |
